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Alliance Protein Laboratories

Alliance Protein Laboratories, a division of KBI Biopharma, is a contract research firm specializing in biophysical analysis. We offer a broad and unique range of biophysical characterization services, including analytical ultracentrifugation (AUC), circular dichroism and fluorescence spectroscopy, light scattering (SEC-MALS and DLS), and DSC. We also offer contract purification services (research scale).

APL is a spin-off from the Protein Chemistry department at Amgen. It was founded in 1998 by Drs. Tsutomu Arakawa and John Philo. Our laboratory is located in San Diego, CA. Our clients include over 400 companies in North America, Europe, Asia, and Australia as well as major universities and non-profit institutes.

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Analytical Ultracentrifugation (AUC)

Price on request

Alliance Protein Laboratories has been offering analytical ultracentrifugation analysis (both sedimentation velocity and sedimentation equilibrium) since 1999. We were the first contract lab in the US to offer these services. APL has completed hundreds of AUC projects on proteins, peptides, nucleic acids, whole viruses, and other... Show more »

Alliance Protein Laboratories has been offering analytical ultracentrifugation analysis (both sedimentation velocity and sedimentation equilibrium) since 1999. We were the first contract lab in the US to offer these services. APL has completed hundreds of AUC projects on proteins, peptides, nucleic acids, whole viruses, and other molecules. At APL all the analytical ultracentrifugation experiments and interpretation are done by our two recognized AUC experts with many publications involving AUC measurements using our two in-house instruments.

Circular dichroism (CD) spectroscopy is an important tool for characterizing the conformation (secondary structure and tertiary structure) and thermal stability of proteins and DNA. It is often used in comparability protocols to demonstrate similarity of molecular conformation. It can be used for:

Circular dichroism (CD) spectroscopy is an important tool for characterizing the conformation (secondary structure and tertiary structure) and thermal stability of proteins and DNA. It is often used in comparability protocols to demonstrate similarity of molecular conformation. It can be used for:

• determining whether a protein is folded, and if so characterizing its secondary structure, tertiary structure, and the structural family to which it belongs

• comparing the structures of a protein obtained from different sources (e.g. species or expression systems) or comparing structures for different mutants of the same protein

• studying the conformational stability of a protein under stress -- thermal stability, pH stability, and stability to denaturants -- and how this stability is altered by buffer composition or addition of stabilizers and excipients

◦ CD is excellent for finding solvent conditions that increase the melting temperature and/or the reversibility of thermal unfolding, conditions which generally enhance shelf life

◦ If there are any conformational changes, this will result in a spectrum which will differ from the sum of the individual components. Small conformational changes have been seen, for example, upon formation of several different receptor/ligand complexes.

Alliance Protein Laboratories has been offering circular dichroism spectroscopy services since 1998 and has completed hundreds of CD analysis projects on proteins, peptides, nucleic acids, and other molecules. At APL all the CD experiments and interpretation are done by Tsutomu Arakawa, a recognized expert with over 25 years experience in biotech product development and over 80 publications involving CD measurements. In 2016 we upgraded to a state-of-the-art Jasco 1500 CD instrument.

APL offers DSC of proteins, nucleic acids, or other macromolecules using an automated MicroCal/Malvern VP-capillary DSC instrument. All DSC experiments, data analysis, and interpretation is done by a Ph.D.-level biophysicist with extensive experience and publications in thermodynamic analysis.

APL offers DSC of proteins, nucleic acids, or other macromolecules using an automated MicroCal/Malvern VP-capillary DSC instrument. All DSC experiments, data analysis, and interpretation is done by a Ph.D.-level biophysicist with extensive experience and publications in thermodynamic analysis.

Alliance Protein Laboratories has been offering light scattering analysis services since 2001. APL scientists introduced SEC-MALS to the biotech industry in 1991, and later pioneered new methods to analyze conjugated proteins (glycoproteins and PEGylated proteins) and deconvolute the masses of the peptide and conjugating species.... Show more »

Alliance Protein Laboratories has been offering light scattering analysis services since 2001. APL scientists introduced SEC-MALS to the biotech industry in 1991, and later pioneered new methods to analyze conjugated proteins (glycoproteins and PEGylated proteins) and deconvolute the masses of the peptide and conjugating species.

A.P.L. has completed scores of SEC-MALS and DLS analysis projects on proteins, peptides, nucleic acids, and other molecules. To our knowledge A.P.L. is the only contract laboratory in the U.S. to offer both of these light scattering methods. At A.P.L. all the light scattering experiments and interpretation are done by these experts who have 28 publications in this area.

For SEC-MALS A.P.L. has a Wyatt Technology miniDAWNâ?¢ TREOS MALS light scattering detector used together with both a refractive index detector (Wyatt Optilab rEX) and a UV absorbance detector. For batch-mode DLS we have a Wyatt Dynapro MS/X with Peltier temperature control. Turn-around for LS analysis is typically 2-4 weeks.

APL can provide intrinsic fluorescence measurements to characterize proteins and to compare the tertiary structure of proteins (comparability protocols) using our Horiba Fluoromax 4 instrument. All experiments and data interpretation are done by a Ph.D.-level biophysicist.

APL can provide intrinsic fluorescence measurements to characterize proteins and to compare the tertiary structure of proteins (comparability protocols) using our Horiba Fluoromax 4 instrument. All experiments and data interpretation are done by a Ph.D.-level biophysicist.

APL. has offered native gel analysis services since 1998. Today many labs unfortunately ignore this valuable tool because they think native gels are just too hard to use, or because they mistakenly believe they can only be used with acidic proteins. At Alliance Protein Laboratories we routinely run native gels on both basic and... Show more »

APL. has offered native gel analysis services since 1998. Today many labs unfortunately ignore this valuable tool because they think native gels are just too hard to use, or because they mistakenly believe they can only be used with acidic proteins. At Alliance Protein Laboratories we routinely run native gels on both basic and acidic proteins. We would be happy to run samples for you and/or work with you to develop a protocol for use in your lab.